ArticleCommunicative & integrative biology2017
Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.
Article in Communicative & integrative biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 27 citations in OpenAlex.
- Healthy rural living: a misplaced optimism? : District-level agricultural index and Parkinson's disease risk in Austria.Wiener klinische Wochenschrift · 2026Article
- ZnJournal of the American Chemical Society · 2025Article
- Metal interactions of α-synuclein probed by NMR amide-proton exchange.Frontiers in chemistry · 2023Article
- Nuclear alpha-synuclein is present in the human brain and is modified in dementia with Lewy bodies.Acta neuropathologica communications · 2022Article
- Membrane insertion exacerbates the α-Synuclein-Cu(II) dopamine oxidase activity: Metallothionein-3 targets and silences all α-synuclein-Cu(II) complexes.Free radical biology & medicine · 2020Article
- Targeting α-synuclein for PD Therapeutics: A Pursuit on All Fronts.Biomolecules · 2020Review
- Case of Early-Onset Parkinson's Disease in a Heterozygous Mutation Carrier of theJournal of personalized medicine · 2019Article
- Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.Coordination chemistry reviews · 2018Article
- Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease.Frontiers in aging neuroscience · 2018Review
- Parkinsonism in Inherited Metabolic Disorders: Key Considerations and Major Features.Frontiers in neurology · 2018Review
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Authors and funding
6 authors at 5 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Copper is one of the metals described to bind the Parkinson disease-related protein α-synuclein (aSyn), and to promote its aggregation. Although histidine at position 50 in the aSyn sequence is one of the most studied copper-anchoring sites, its precise role in copper binding and aSyn aggregation is still unclear. Previous studies suggested that this residue does not significantly affect copper-mediated aSyn aggregation. However, our findings showed that the aggregation of the pathological H50Q aSyn mutant is enhanced by copper hints otherwise. Despite the inexistence of a model for aSyn H50Q-copper complexation, we discuss possible mechanisms by which this metal contributes to the misfolding and self-assembly of this particular aSyn mutant. Considering the genetic association of the H50Q mutation with familial forms of Parkinson disease, and the fact that copper homeostasis is deregulated in this disorder, understanding the interplay between both factors will shed light into the molecular and cellular mechanisms triggering the development and spreading of the aSyn pathology.
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